Targeting these sticky proteins with drugs is difficult, however, as plasmodia contain many different varieties, which they use to evade the human immune system. However, certain parts of the protein have to remain constant for proper function, and in this study, Matthew Higgins generated high-resolution 3-D structures of a malarial sticky protein that binds to placenta, PfEMP1, to detail how plasmodia protect these conserved areas. Higgins found that a variable region of PfEMP1 covers a section that is important for docking up with the placental wall. When the infected RBC gets close to chondroitin sulphate, a structural molecule on blood vessels, the variable region moves aside and ever so briefly exposes the binding region, just enough to allow anchoring to take place. Higgins notes that women in regions where malaria is endemic do gain some immunity to the build-up of RBCs at the placenta after multiple pregnancies by developing an immune response for PfEMP1. Targeting this conserved binding domain of the protein with pharmaceuticals that mimic chondroitin sulphate and expose this region might be an approach to hasten this immunity.
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